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Q05921

- RN5A_MOUSE

UniProt

Q05921 - RN5A_MOUSE

Protein

2-5A-dependent ribonuclease

Gene

Rnasel

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (11 Feb 2002)
      Previous versions | rss
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    Functioni

    Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. Might play a central role in the regulation of mRNA turnover By similarity.By similarity

    Catalytic activityi

    Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length.

    Cofactori

    Manganese or magnesium. Required for optimal RNA cleavage rates.

    Enzyme regulationi

    After binding to 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) the homodimerization and subsequent activation occurs. Inhibited by RNASEL inhibitor ABCE1/RLI, a cytoplasmic member of the ATP-binding cassette (ABC) transporter family By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri401 – 43636C6-typeSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. endonuclease activity Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. protein kinase activity Source: InterPro
    5. ribonuclease activity Source: Ensembl
    6. rRNA binding Source: Ensembl

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-KW
    2. mRNA processing Source: InterPro
    3. negative regulation of viral genome replication Source: Ensembl
    4. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. rRNA processing Source: Ensembl

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    Antiviral defense

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-5A-dependent ribonuclease (EC:3.1.26.-)
    Short name:
    2-5A-dependent RNase
    Alternative name(s):
    Ribonuclease 4
    Ribonuclease L
    Short name:
    RNase L
    Gene namesi
    Name:Rnasel
    Synonyms:Rns4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1098272. Rnasel.

    Subcellular locationi

    Cytoplasm 1 Publication. Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. nuclear matrix Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7357352-5A-dependent ribonucleasePRO_0000067052Add
    BLAST

    Proteomic databases

    MaxQBiQ05921.
    PaxDbiQ05921.
    PRIDEiQ05921.

    PTM databases

    PhosphoSiteiQ05921.

    Expressioni

    Tissue specificityi

    Expressed in spleen, thymus, lung, testis, kidney, liver and heart.

    Inductioni

    By interferons. Virus replication in higher vertebrates is restrained by IFNs that cause cells to transcribe genes encoding antiviral proteins, such as 2'-5' oligoadenylate synthetases (OASs). oligoadenylate synthetase is stimulated by dsRNA to produce 5'-phosphorylated, 2'-5'-linked oligoadenylates (2-5A), whose function is to activate RNASEL.

    Gene expression databases

    ArrayExpressiQ05921.
    BgeeiQ05921.
    GenevestigatoriQ05921.

    Interactioni

    Subunit structurei

    Monomer (inactive form) or homodimer. Interacts with ABCE1; this interaction inhibits the RNASEL By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ05921.
    SMRiQ05921. Positions 25-717.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati24 – 5330ANK 1Add
    BLAST
    Repeati58 – 8730ANK 2Add
    BLAST
    Repeati91 – 12030ANK 3Add
    BLAST
    Repeati124 – 15330ANK 4Add
    BLAST
    Repeati167 – 19731ANK 5Add
    BLAST
    Repeati201 – 23434ANK 6Add
    BLAST
    Repeati238 – 26831ANK 7Add
    BLAST
    Repeati272 – 30130ANK 8Add
    BLAST
    Repeati303 – 32826ANK 9Add
    BLAST
    Domaini364 – 584221Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini587 – 722136KENPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni229 – 242142-5A binding (P-loop) 1Add
    BLAST
    Regioni253 – 275232-5A binding (P-loop) 2Add
    BLAST

    Domaini

    The nine ankyrin repeats also called 2-5A sensor constitute the N-terminus 2-5A binding domain.
    The protein kinase domain is predicted to be catalytically inactive. It allows the homodimerization.
    The ribonuclease domain is located in the C-terminus. A single active nuclease domain in a dimer is sufficient for ribonuclease activity.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily.Curated
    Contains 9 ANK repeats.PROSITE-ProRule annotation
    Contains 1 KEN domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri401 – 43636C6-typeSequence AnalysisAdd
    BLAST

    Keywords - Domaini

    ANK repeat, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0666.
    GeneTreeiENSGT00750000117792.
    HOGENOMiHOG000276879.
    HOVERGENiHBG012673.
    InParanoidiQ05921.
    KOiK01165.
    OMAiDCGDLVM.
    OrthoDBiEOG7VDXNN.
    PhylomeDBiQ05921.
    TreeFamiTF344032.

    Family and domain databases

    Gene3Di1.25.40.20. 3 hits.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR010513. KEN_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR006567. PUG-dom.
    [Graphical view]
    PfamiPF00023. Ank. 6 hits.
    PF00069. Pkinase. 1 hit.
    PF06479. Ribonuc_2-5A. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 8 hits.
    SM00580. PUG. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 7 hits.
    PS51392. KEN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q05921-1 [UniParc]FASTAAdd to Basket

    « Hide

    METPDYNTPQ GGTPSAGSQR TVVEDDSSLI KAVQKGDVVR VQQLLEKGAD    50
    ANACEDTWGW TPLHNAVQAG RVDIVNLLLS HGADPHRRKK NGATPFIIAG 100
    IQGDVKLLEI LLSCGADVNE CDENGFTAFM EAAERGNAEA LRFLFAKGAN 150
    VNLRRQTTKD KRRLKQGGAT ALMSAAEKGH LEVLRILLND MKAEVDARDN 200
    MGRNALIRTL LNWDCENVEE ITSILIQHGA DVNVRGERGK TPLIAAVERK 250
    HTGLVQMLLS REGINIDARD NEGKTALLIA VDKQLKEIVQ LLLEKGADKC 300
    DDLVWIARRN HDYHLVKLLL PYVANPDTDP PAGDWSPHSS RWGTALKSLH 350
    SMTRPMIGKL KIFIHDDYKI AGTSEGAVYL GIYDNREVAV KVFRENSPRG 400
    CKEVSCLRDC GDHSNLVAFY GREDDKGCLY VCVSLCEWTL EEFLRLPREE 450
    PVENGEDKFA HSILLSIFEG VQKLHLHGYS HQDLQPQNIL IDSKKAVRLA 500
    DFDQSIRWMG ESQMVRRDLE DLGRLVLYVV MKGEIPFETL KTQNDEVLLT 550
    MSPDEETKDL IHCLFSPGEN VKNCLVDLLG HPFFWTWENR YRTLRNVGNE 600
    SDIKVRKCKS DLLRLLQHQT LEPPRSFDQW TSKIDKNVMD EMNHFYEKRK 650
    KNPYQDTVGD LLKFIRNIGE HINEEKKRGM KEILGDPSRY FQETFPDLVI 700
    YIYKKLKETE YRKHFPQPPP RLSVPEAVGP GGIQS 735
    Length:735
    Mass (Da):83,275
    Last modified:February 11, 2002 - v2
    Checksum:iB6632F4A5B50F711
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF281045 mRNA. Translation: AAG33708.1.
    L10382 Genomic DNA. Translation: AAA37117.1.
    CCDSiCCDS15377.1.
    PIRiB45771.
    RefSeqiNP_036012.1. NM_011882.2.
    XP_006529588.1. XM_006529525.1.
    XP_006529589.1. XM_006529526.1.
    XP_006529590.1. XM_006529527.1.
    XP_006529591.1. XM_006529528.1.
    XP_006529592.1. XM_006529529.1.
    XP_006529593.1. XM_006529530.1.
    UniGeneiMm.259254.

    Genome annotation databases

    EnsembliENSMUST00000086209; ENSMUSP00000083385; ENSMUSG00000066800.
    ENSMUST00000182538; ENSMUSP00000138734; ENSMUSG00000066800.
    GeneIDi24014.
    KEGGimmu:24014.
    UCSCiuc007daf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF281045 mRNA. Translation: AAG33708.1 .
    L10382 Genomic DNA. Translation: AAA37117.1 .
    CCDSi CCDS15377.1.
    PIRi B45771.
    RefSeqi NP_036012.1. NM_011882.2.
    XP_006529588.1. XM_006529525.1.
    XP_006529589.1. XM_006529526.1.
    XP_006529590.1. XM_006529527.1.
    XP_006529591.1. XM_006529528.1.
    XP_006529592.1. XM_006529529.1.
    XP_006529593.1. XM_006529530.1.
    UniGenei Mm.259254.

    3D structure databases

    ProteinModelPortali Q05921.
    SMRi Q05921. Positions 25-717.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q05921.
    ChEMBLi CHEMBL2687.

    PTM databases

    PhosphoSitei Q05921.

    Proteomic databases

    MaxQBi Q05921.
    PaxDbi Q05921.
    PRIDEi Q05921.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000086209 ; ENSMUSP00000083385 ; ENSMUSG00000066800 .
    ENSMUST00000182538 ; ENSMUSP00000138734 ; ENSMUSG00000066800 .
    GeneIDi 24014.
    KEGGi mmu:24014.
    UCSCi uc007daf.1. mouse.

    Organism-specific databases

    CTDi 6041.
    MGIi MGI:1098272. Rnasel.

    Phylogenomic databases

    eggNOGi COG0666.
    GeneTreei ENSGT00750000117792.
    HOGENOMi HOG000276879.
    HOVERGENi HBG012673.
    InParanoidi Q05921.
    KOi K01165.
    OMAi DCGDLVM.
    OrthoDBi EOG7VDXNN.
    PhylomeDBi Q05921.
    TreeFami TF344032.

    Miscellaneous databases

    NextBioi 303947.
    PROi Q05921.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05921.
    Bgeei Q05921.
    Genevestigatori Q05921.

    Family and domain databases

    Gene3Di 1.25.40.20. 3 hits.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR010513. KEN_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR006567. PUG-dom.
    [Graphical view ]
    Pfami PF00023. Ank. 6 hits.
    PF00069. Pkinase. 1 hit.
    PF06479. Ribonuc_2-5A. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 8 hits.
    SM00580. PUG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 7 hits.
    PS51392. KEN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis and origins of the human and mouse RNase L genes: mediators of interferon action."
      Zhou A., Nie H., Silverman R.H.
      Mamm. Genome 11:989-992(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C3H/An.
      Tissue: Adipose tissue.
    2. "Expression cloning of 2-5A-dependent RNAase: a uniquely regulated mediator of interferon action."
      Zhou A., Hassel B.A., Silverman R.H.
      Cell 72:753-765(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-679.
    3. "The 2-5A/RNase L/RNase L inhibitor (RNI) pathway regulates mitochondrial mRNAs stability in interferon alpha-treated H9 cells."
      Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B., Salehzada T.
      J. Biol. Chem. 276:48473-48482(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    4. Erratum
      Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B., Salehzada T.
      J. Biol. Chem. 277:13354-13354(2002)

    Entry informationi

    Entry nameiRN5A_MOUSE
    AccessioniPrimary (citable) accession number: Q05921
    Secondary accession number(s): Q9ERU7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: February 11, 2002
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3